What units should I use?

You can use any consistent units — mM for [S] and µmol/min for v, for example. The calculator is unit-agnostic; the reported Km will be in the same units as [S] and Vmax in the same units as v.

Why do I need at least three data points?

Linear regression requires at least two points to define a line, but three or more points are needed to assess linearity and get a meaningful R² value.

What does a high R² mean?

An R² close to 1 indicates the transformed data fit the Lineweaver-Burk model well, supporting Michaelis-Menten kinetics. A low R² suggests non-linear behavior, cooperativity, or experimental error.

Can this detect inhibition?

Yes indirectly. Competitive inhibition increases the apparent Km while Vmax stays the same; uncompetitive inhibition decreases both; non-competitive inhibition decreases Vmax while Km remains unchanged. Compare runs with and without inhibitor.

What are the limitations of the Lineweaver-Burk plot?

The double-reciprocal transformation amplifies errors at low substrate concentrations (high 1/[S] values). For precise parameter estimation, non-linear regression on the original Michaelis-Menten curve is preferred.

Lineweaver-Burk Calculator

Enter substrate concentration and reaction velocity pairs to compute Km and Vmax via the Lineweaver-Burk double-reciprocal linearization.

Enter Kinetics Data

Add at least 3 rows. [S] and v must be positive numbers.

[S] (substrate)	v (velocity)

Enter data and click Calculate to see the plot

Transformed Data (1/[S] vs 1/v)

[S]	v	1/[S]	1/v

Summary

The Lineweaver-Burk calculator applies the double-reciprocal transformation (1/v vs 1/[S]) to your enzyme kinetics data to linearize the Michaelis-Menten equation. A linear regression on the transformed data yields the slope (Km/Vmax) and y-intercept (1/Vmax), from which Km and Vmax are derived. This approach is widely used in biochemistry courses and labs to characterize enzyme behavior and identify inhibition types.

How it works

Enter at least three [S] / v data pairs in the table (substrate concentration and reaction velocity).
The tool computes 1/[S] and 1/v for each row.
A least-squares linear regression fits a line to the double-reciprocal data.
The y-intercept equals 1/Vmax and the slope equals Km/Vmax.
Km and Vmax are calculated and displayed alongside the regression line equation.
A scatter plot with the fitted line is drawn for visual inspection.

Use cases

Determine Km and Vmax from experimental enzyme assay data.
Visualize linearity of the Michaelis-Menten model for a given dataset.
Cross-check manual double-reciprocal calculations in biochemistry coursework.
Compare kinetic parameters before and after adding an inhibitor.
Prepare a publication-quality Lineweaver-Burk plot description.
Validate pipetting accuracy by checking fit quality (R²).

Frequently Asked Questions

Last updated: 2026-09-30 · Reviewed by Nham Vu